메뉴 건너뛰기




Volumn 50, Issue 3, 2003, Pages 464-473

Comparative properties of a three-dimensional model of Plasmodium falciparum ornithine decarboxylase

Author keywords

Homology model; Malaria; Ornithine decarboxylase; Polyamines

Indexed keywords

ORNITHINE DECARBOXYLASE; POLYAMINE;

EID: 0037441470     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10274     Document Type: Article
Times cited : (17)

References (49)
  • 2
    • 0026671825 scopus 로고
    • Ornithine decarboxylase as an enzyme target for therapy
    • McCann PP, Pegg AE. Ornithine decarboxylase as an enzyme target for therapy. Pharmacol Ther 1992;54:195-215.
    • (1992) Pharmacol Ther , vol.54 , pp. 195-215
    • McCann, P.P.1    Pegg, A.E.2
  • 3
    • 0028956729 scopus 로고
    • Polyamines as targets for therapeutic intervention
    • Marton LJ, Pegg AE. Polyamines as targets for therapeutic intervention. Annu Rev Pharmacol Toxicol 1995;35:55-91.
    • (1995) Annu Rev Pharmacol Toxicol , vol.35 , pp. 55-91
    • Marton, L.J.1    Pegg, A.E.2
  • 4
    • 0028949538 scopus 로고
    • Molecular mechanisms and therapeutic approaches to the treatment of African trypanosomiasis
    • Wang CC. Molecular mechanisms and therapeutic approaches to the treatment of African trypanosomiasis. Annu Rev Pharmacol Toxicol 1995;35:93-127.
    • (1995) Annu Rev Pharmacol Toxicol , vol.35 , pp. 93-127
    • Wang, C.C.1
  • 5
    • 0021127290 scopus 로고
    • Polyamine levels and the activity of their biosynthetic enzymes in human erythrocytes infected with the malaria parasite, Plasmodium falciparum
    • Assaraf YG, Golenser J, Spira DT, Bachrach U. Polyamine levels and the activity of their biosynthetic enzymes in human erythrocytes infected with the malaria parasite, Plasmodium falciparum. Biochem J 1984;222:815-819.
    • (1984) Biochem J , vol.222 , pp. 815-819
    • Assaraf, Y.G.1    Golenser, J.2    Spira, D.T.3    Bachrach, U.4
  • 6
    • 0023085302 scopus 로고
    • Cytostatic effect of DL-αμdiflouromethylornithine against Plasmodium falciparum and its reversal by diamines and spermidine
    • Assaraf YG, Golenser J, Spira DT, Messer G, Bachrach U. Cytostatic effect of DL-αμdiflouromethylornithine against Plasmodium falciparum and its reversal by diamines and spermidine. Parasitol Res 1987b;73:313-318.
    • (1987) Parasitol Res , vol.73 , pp. 313-318
    • Assaraf, Y.G.1    Golenser, J.2    Spira, D.T.3    Messer, G.4    Bachrach, U.5
  • 7
    • 0023433861 scopus 로고
    • Plasmodium falciparum and Plasmodium berghei: Effects of ornithine decarboxylase inhibitors on erythrocytic schizogony
    • Bitoni AJ, McCann PP, Sjoerdsma A. Plasmodium falciparum and Plasmodium berghei: effects of ornithine decarboxylase inhibitors on erythrocytic schizogony. Exp Parasitol 1987;64:237-243.
    • (1987) Exp Parasitol , vol.64 , pp. 237-243
    • Bitoni, A.J.1    McCann, P.P.2    Sjoerdsma, A.3
  • 8
    • 0000731846 scopus 로고
    • Bis(benzyl)polyamine analogs inhibit the growth of chloroquine- resistant human malaria parasites (Plasmodium falciparum) in vitro and in combination with alpha-difluoromethylornithine cure murine malaria
    • Bitonti AJ, Dumont JA, Bush TL, Edwards ML, Stemerick DM, McCann PP, Sjoerdsma A. Bis(benzyl)polyamine analogs inhibit the growth of chloroquine- resistant human malaria parasites (Plasmodium falciparum) in vitro and in combination with alpha-difluoromethylornithine cure murine malaria. Proc Natl Acad Sci USA 1989;86:651-655.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 651-655
    • Bitonti, A.J.1    Dumont, J.A.2    Bush, T.L.3    Edwards, M.L.4    Stemerick, D.M.5    McCann, P.P.6    Sjoerdsma, A.7
  • 9
    • 0025844981 scopus 로고
    • Disruption of Plasmodium falciparum-infected erythrocyte cytoadherence to human melanoma cells with inhibitors of glycoprotein processing
    • Wright PS, Cross-Doersen DE, Schroeder KK, Bowlin TL, McCann PP, Bitonti AJ. Disruption of Plasmodium falciparum-infected erythrocyte cytoadherence to human melanoma cells with inhibitors of glycoprotein processing. Biochem Pharmacol 1991;41:1855-1861.
    • (1991) Biochem Pharmacol , vol.41 , pp. 1855-1861
    • Wright, P.S.1    Cross-Doersen, D.E.2    Schroeder, K.K.3    Bowlin, T.L.4    McCann, P.P.5    Bitonti, A.J.6
  • 10
    • 0039765384 scopus 로고    scopus 로고
    • In the human malaria parasite Plasmodium falciparum, polyamines are synthesized by a bifunctional ornithine decarboxylase, S-adenosylmethionine decarboxylase
    • Muller S, Da'dara A, Luersen K, Wrenger C, Das Gupta R, Madhubala R, Walter RD. In the human malaria parasite Plasmodium falciparum, polyamines are synthesized by a bifunctional ornithine decarboxylase, S-adenosylmethionine decarboxylase. J Biol Chem 2000;275:8097-8102.
    • (2000) J Biol Chem , vol.275 , pp. 8097-8102
    • Muller, S.1    Da'dara, A.2    Luersen, K.3    Wrenger, C.4    Das Gupta, R.5    Madhubala, R.6    Walter, R.D.7
  • 11
    • 2242478824 scopus 로고
    • Characterisation of ornithine decarboxylase from various sources
    • Hayashi S, Hayashi S, editors. Oxford, England: Pergamon Press, Inc.
    • Pegg AE. Characterisation of ornithine decarboxylase from various sources. In: Hayashi S, Hayashi S, editors. Ornithine decarboxylase: biology, enzymology and molecular genetics. Oxford, England: Pergamon Press, Inc.; 1989. p 21-28.
    • (1989) Ornithine Decarboxylase: Biology, Enzymology and Molecular Genetics , pp. 21-28
    • Pegg, A.E.1
  • 12
    • 0034614359 scopus 로고    scopus 로고
    • Crystal structure of human ornithine decarboxylase at 2.1 A resolution: Structural insights to antizyme binding
    • Almrud JJ, Oliveira MA, Kern AD, Grishin NV, Phillips MA, Hackert ML. Crystal structure of human ornithine decarboxylase at 2.1 A resolution: structural insights to antizyme binding. J Mol Biol 2000;295:7-16.
    • (2000) J Mol Biol , vol.295 , pp. 7-16
    • Almrud, J.J.1    Oliveira, M.A.2    Kern, A.D.3    Grishin, N.V.4    Phillips, M.A.5    Hackert, M.L.6
  • 13
    • 0033576286 scopus 로고    scopus 로고
    • X-ray structure of ornithine decarboxylase from Trypanosoma brucei: The native structure and the structure in complex with alpha-difluoromethylornithine
    • Grishin NV, Osterman AL, Brooks HB, Phillips MA, Goldsmith EJ. X-ray structure of ornithine decarboxylase from Trypanosoma brucei: the native structure and the structure in complex with alpha-difluoromethylornithine. Biochemistry 1999;38:15174-15184.
    • (1999) Biochemistry , vol.38 , pp. 15174-15184
    • Grishin, N.V.1    Osterman, A.L.2    Brooks, H.B.3    Phillips, M.A.4    Goldsmith, E.J.5
  • 14
    • 0029131487 scopus 로고
    • Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 A resolution
    • Momany C, Ernst S, Ghosh R, Chang NL, Hackert ML. Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 A resolution. J Mol Biol 1995;252:643-655.
    • (1995) J Mol Biol , vol.252 , pp. 643-655
    • Momany, C.1    Ernst, S.2    Ghosh, R.3    Chang, N.L.4    Hackert, M.L.5
  • 15
    • 0033395809 scopus 로고    scopus 로고
    • Three-dimensional structure of the Gly121Tyr dimeric form of ornithine decarboxylase from Lactobacillus 30a
    • Vitali J, Carroll D, Chaudhry RG, Hackert ML. Three-dimensional structure of the Gly121Tyr dimeric form of ornithine decarboxylase from Lactobacillus 30a. Acta Crystallogr D Biol Crystallogr 1999;55:1978-1985.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , pp. 1978-1985
    • Vitali, J.1    Carroll, D.2    Chaudhry, R.G.3    Hackert, M.L.4
  • 16
    • 0033135202 scopus 로고    scopus 로고
    • Structure of mammalian ornithine decarboxylase at 1.6 A resolution: Stereo-chemical implications of PLP-dependent amino acid decarboxylases
    • Kern AD, Oliveira MA, Coffino P, Hackert ML. Structure of mammalian ornithine decarboxylase at 1.6 A resolution: stereo-chemical implications of PLP-dependent amino acid decarboxylases. Struct Fold Des 1999;7:567-581.
    • (1999) Struct Fold Des , vol.7 , pp. 567-581
    • Kern, A.D.1    Oliveira, M.A.2    Coffino, P.3    Hackert, M.L.4
  • 17
    • 0033134691 scopus 로고    scopus 로고
    • The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold
    • Ekstrom JL, Mathews II, Stanley BA, Pegg AE, Ealick SE. The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold. Struct Fold Des 1999;7:583-595.
    • (1999) Struct Fold Des , vol.7 , pp. 583-595
    • Ekstrom, J.L.1    Mathews, I.I.2    Stanley, B.A.3    Pegg, A.E.4    Ealick, S.E.5
  • 18
    • 0033999271 scopus 로고    scopus 로고
    • Overcoming codon bias: A method for highlevel over-expression of Plasmodium and other AT-rich parasite genes in Eschericia coli
    • Baca AM, Hol WG. Overcoming codon bias: a method for highlevel over-expression of Plasmodium and other AT-rich parasite genes in Eschericia coli. Int J Parasitol 2000;30:113-118.
    • (2000) Int J Parasitol , vol.30 , pp. 113-118
    • Baca, A.M.1    Hol, W.G.2
  • 19
    • 0028244256 scopus 로고
    • Expression systems to best mimick the native structure
    • Chang SP. Expression systems to best mimick the native structure. Am J Trop Med Hyg 1994;50:20-26.
    • (1994) Am J Trop Med Hyg , vol.50 , pp. 20-26
    • Chang, S.P.1
  • 21
    • 0033051342 scopus 로고    scopus 로고
    • Towards an understanding of drug resistance in malaria: Three-dimensional structure of Plasmodium falciparum dihydrofolate reductase by homology building
    • Lemcke T, Christensen IT, Jorgensen FS. Towards an understanding of drug resistance in malaria: three-dimensional structure of Plasmodium falciparum dihydrofolate reductase by homology building. Bioorg Med Chem 1999;7:1003-1011.
    • (1999) Bioorg Med Chem , vol.7 , pp. 1003-1011
    • Lemcke, T.1    Christensen, I.T.2    Jorgensen, F.S.3
  • 22
    • 0031587932 scopus 로고    scopus 로고
    • Lead discovery of inhibitors of the dihydrofolate reductase domain of Plasmodium falciparum dihydrofolate reductase-thymidylate synthase
    • Toyoda T, Brobey RK, Sano G, Horii T, Tomioka N, Itai A. Lead discovery of inhibitors of the dihydrofolate reductase domain of Plasmodium falciparum dihydrofolate reductase-thymidylate synthase. Biochem Biophys Res Commun 1997;235:515-519.
    • (1997) Biochem Biophys Res Commun , vol.235 , pp. 515-519
    • Toyoda, T.1    Brobey, R.K.2    Sano, G.3    Horii, T.4    Tomioka, N.5    Itai, A.6
  • 23
    • 0031734331 scopus 로고    scopus 로고
    • Antimalaria drug discovery: Development of inhibitors of dihydrofolate reductase active in drug resistance
    • Warhurst DC. Antimalaria drug discovery: development of inhibitors of dihydrofolate reductase active in drug resistance. Drug Discov Today 1998;3:538-546.
    • (1998) Drug Discov Today , vol.3 , pp. 538-546
    • Warhurst, D.C.1
  • 25
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 26
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N, Peitsch MC. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997;18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 28
    • 0001787027 scopus 로고    scopus 로고
    • Molecular modelling of proteins
    • Guex N, Peitsch MC. Molecular modelling of proteins. Immunol News 1999;6:132-134.
    • (1999) Immunol News , vol.6 , pp. 132-134
    • Guex, N.1    Peitsch, M.C.2
  • 29
    • 0029091171 scopus 로고
    • Comparative molecular modelling of the Fas-ligand and other members of the TNF family
    • Peitsch MC, Tschopp J. Comparative molecular modelling of the Fas-ligand and other members of the TNF family. Mol Immunol 1995;32:761-772.
    • (1995) Mol Immunol , vol.32 , pp. 761-772
    • Peitsch, M.C.1    Tschopp, J.2
  • 30
    • 0029004590 scopus 로고
    • Protein modelling by E-mail
    • Peitsch MC. Protein modelling by E-mail. Bio/Technology 1995;13:658-660.
    • (1995) Bio/Technology , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 31
    • 0030053370 scopus 로고    scopus 로고
    • ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling
    • Peitsch MC. ProMod and Swiss-Model: internet-based tools for automated comparative protein modelling. Biochem Soc Trans 1996;24:274-279.
    • (1996) Biochem Soc Trans , vol.24 , pp. 274-279
    • Peitsch, M.C.1
  • 32
    • 0030451549 scopus 로고    scopus 로고
    • Automated modelling of the transmembrane region of G-protein coupled receptor by Swiss-model
    • Peitsch MC, Herzyk P, Wells TN, Hubbard RE. Automated modelling of the transmembrane region of G-protein coupled receptor by Swiss-model. Receptors Channels 1996;4:161-164.
    • (1996) Receptors Channels , vol.4 , pp. 161-164
    • Peitsch, M.C.1    Herzyk, P.2    Wells, T.N.3    Hubbard, R.E.4
  • 33
    • 44949272730 scopus 로고
    • A time-efficient linear-space local similarity algorithm
    • Huang X, Miller W. A time-efficient linear-space local similarity algorithm. Adv Appl Math 1991;12:337.
    • (1991) Adv Appl Math , vol.12 , pp. 337
    • Huang, X.1    Miller, W.2
  • 34
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modelling and drug design program
    • Vriend G. WHAT IF: a molecular modelling and drug design program. J Mol Graph 1990;8:52-56.
    • (1990) J Mol Graph , vol.8 , pp. 52-56
    • Vriend, G.1
  • 35
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacAthur MW, Moss DS, Thorton JM. PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 1993;29:283-291.
    • (1993) J Appl Crystallogr , vol.29 , pp. 283-291
    • Laskowski, R.A.1    MacAthur, M.W.2    Moss, D.S.3    Thorton, J.M.4
  • 36
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991;11:281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 38
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 1995;247:536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 39
    • 0029901640 scopus 로고    scopus 로고
    • Analysis of compositionallz baised regions in sequence databases
    • Wooton JC, Federhen S. Analysis of compositionallz baised regions in sequence databases. Methods Enzymol 1996;266:554-571.
    • (1996) Methods Enzymol , vol.266 , pp. 554-571
    • Wooton, J.C.1    Federhen, S.2
  • 40
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace AC, Laskowski RA, Thorton JM. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng 1995;8:127-134.
    • (1995) Protein Eng , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thorton, J.M.3
  • 41
    • 0027504342 scopus 로고
    • Effects of mutations at active site residues on the activity of ornithine decarboxylase and its inhibition by active site directed irreversible inhibitors
    • Coleman CS, Stanley BA, Pegg AE. Effects of mutations at active site residues on the activity of ornithine decarboxylase and its inhibition by active site directed irreversible inhibitors. J Biol Chem 1993;268:24572-24579.
    • (1993) J Biol Chem , vol.268 , pp. 24572-24579
    • Coleman, C.S.1    Stanley, B.A.2    Pegg, A.E.3
  • 42
    • 0028067923 scopus 로고
    • Formation of functional cross-species heterodimers of ornithine decarboxylase
    • Osterman A, Grishin NV, Kinch LN, Phillips MA. Formation of functional cross-species heterodimers of ornithine decarboxylase. Biochemistry 1994;33:13662-13667.
    • (1994) Biochemistry , vol.33 , pp. 13662-13667
    • Osterman, A.1    Grishin, N.V.2    Kinch, L.N.3    Phillips, M.A.4
  • 43
    • 0035104190 scopus 로고    scopus 로고
    • Low-complexity regions in Plasmodium falciparum proteins
    • Pizzi E, Frontali C. Low-complexity regions in Plasmodium falciparum proteins. Genome Res 2001;11:218-229.
    • (2001) Genome Res , vol.11 , pp. 218-229
    • Pizzi, E.1    Frontali, C.2
  • 45
    • 0028071986 scopus 로고
    • Ornithine decarboxylase: Structure, function and translational regulation
    • Pegg AE, Shantz LM, Coleman CS. Ornithine decarboxylase: structure, function and translational regulation. Biochem Soc Trans 1994;22:846-852.
    • (1994) Biochem Soc Trans , vol.22 , pp. 846-852
    • Pegg, A.E.1    Shantz, L.M.2    Coleman, C.S.3
  • 46
    • 0035839493 scopus 로고    scopus 로고
    • The Plasmodium falciparum bifunctional ornithine decarboxylase, S-adenosylmethionine decarboxylase enables a well balanced polyamine synthesis without domain-domain interaction
    • Wrenger C, Luersen K, Krause T, Muller S, Walter RD. The Plasmodium falciparum bifunctional ornithine decarboxylase, S-adenosylmethionine decarboxylase enables a well balanced polyamine synthesis without domain-domain interaction. J Biol Chem 2001;276:29651-29656.
    • (2001) J Biol Chem , vol.276 , pp. 29651-29656
    • Wrenger, C.1    Luersen, K.2    Krause, T.3    Muller, S.4    Walter, R.D.5
  • 47
    • 0034534695 scopus 로고    scopus 로고
    • The ornithine decarboxylase domain of the bifunctional ornithine decarboxylase/S-adenosylemethionine decarboxylase of Plasmodium falciparum: Recombinant expression and catalytic properties of two different constructs
    • Krause T, Luersen K, Wrenger C, Gilberger TW, Muller S, Walter RD. The ornithine decarboxylase domain of the bifunctional ornithine decarboxylase/S-adenosylemethionine decarboxylase of Plasmodium falciparum: recombinant expression and catalytic properties of two different constructs. Biochem J 2000;352:287-292.
    • (2000) Biochem J , vol.352 , pp. 287-292
    • Krause, T.1    Luersen, K.2    Wrenger, C.3    Gilberger, T.W.4    Muller, S.5    Walter, R.D.6
  • 49
    • 0026740249 scopus 로고
    • 2-Substituted 3-(aminoozy)propanamines as inhibitors of ornithine decarboxylase: Synthesis and biological activity
    • Standek J, Frei J, Schneider P, Regenass U. 2-Substituted 3-(aminoozy)propanamines as inhibitors of ornithine decarboxylase: synthesis and biological activity. J Med Chem 1992;35:1339-1344.
    • (1992) J Med Chem , vol.35 , pp. 1339-1344
    • Standek, J.1    Frei, J.2    Schneider, P.3    Regenass, U.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.